RPOA_ECOLI
ID RPOA_ECOLI Reviewed; 329 AA.
AC P0A7Z4; P00574; Q2M6W0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DNA-directed RNA polymerase subunit alpha;
DE Short=RNAP subunit alpha;
DE EC=2.7.7.6;
DE AltName: Full=RNA polymerase subunit alpha;
DE AltName: Full=Transcriptase subunit alpha;
GN Name=rpoA; Synonyms=pez, phs, sez; OrderedLocusNames=b3295, JW3257;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=323055; DOI=10.1016/0014-5793(77)80131-2;
RA Ovchinnikov Y.A., Lipkin V.M., Modyanov N.N., Chertov O.Y., Smirnov Y.V.;
RT "Primary structure of alpha-subunit of DNA-dependent RNA polymerase from
RT Escherichia coli.";
RL FEBS Lett. 76:108-111(1977).
RN [2]
RP PROTEIN SEQUENCE.
RA Modyanov N.N., Lipkin V.M., Smirnov Y.V., Shuvaeva T.M.,
RA Kocherginskaya S.A.;
RT "The primary structure of alpha-subunit of DNA-dependent RNA polymerase
RT from E. coli. V. The cyanogen bromide peptides.";
RL Bioorg. Khim. 4:437-449(1978).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6379605; DOI=10.1093/nar/12.14.5813;
RA Meek D.W., Hayward R.S.;
RT "Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second
RT regulatory binding site for protein S4?";
RL Nucleic Acids Res. 12:5813-5821(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2989779; DOI=10.1093/nar/13.11.3891;
RA Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H.,
RA Zengel J.M., Lindahl L.;
RT "Nucleotide sequence of the alpha ribosomal protein operon of Escherichia
RT coli.";
RL Nucleic Acids Res. 13:3891-3903(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, SUBUNIT, AND MUTAGENESIS OF
RP ARG-45 AND ARG-191.
RC STRAIN=K12;
RX PubMed=2235479; DOI=10.1093/nar/18.20.5945;
RA Igarashi K., Fujita N., Ishihama A.;
RT "Sequence analysis of two temperature-sensitive mutations in the alpha
RT subunit gene (rpoA) of Escherichia coli RNA polymerase.";
RL Nucleic Acids Res. 18:5945-5948(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159.
RX PubMed=387752; DOI=10.1016/s0021-9258(19)86562-6;
RA Post L.E., Nomura M.;
RT "Nucleotide sequence of the intercistronic region preceding the gene for
RT RNA polymerase subunit alpha in Escherichia coli.";
RL J. Biol. Chem. 254:10604-10606(1979).
RN [9]
RP PROTEIN SEQUENCE OF 1-19.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RC STRAIN=K12;
RX PubMed=3894886; DOI=10.1007/bf00330268;
RA Schnier J., Isono S., Cumberlidge A.G., Isono K.;
RT "Unstable mutations caused by regional tandem multiplications in the gene
RT for ribosomal protein S4 show thermosensitivity in Escherichia coli.";
RL Mol. Gen. Genet. 199:265-270(1985).
RN [11]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12;
RX PubMed=1095419; DOI=10.1016/0014-5793(75)81001-5;
RA Fujiki H., Zurek G.;
RT "The subunits of DNA-dependent RNA polymerase from E. coli: I. Amino acid
RT analysis and primary structure of the N-terminal regions.";
RL FEBS Lett. 55:242-244(1975).
RN [12]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [13]
RP FUNCTION IN TRANSCRIPTION, PROBABLE INTERACTION WITH CRP, SUBUNIT, AND
RP DOMAIN.
RX PubMed=1646077; DOI=10.1016/0092-8674(91)90553-b;
RA Igarashi K., Ishihama A.;
RT "Bipartite functional map of the E. coli RNA polymerase alpha subunit:
RT involvement of the C-terminal region in transcription activation by cAMP-
RT CRP.";
RL Cell 65:1015-1022(1991).
RN [14]
RP INTERACTION WITH CRP, AND MUTAGENESIS OF 162-GLU--GLU-165 AND GLU-165.
RX PubMed=8978616; DOI=10.1016/s0092-8674(00)81806-1;
RA Niu W., Kim Y., Tau G., Heyduk T., Ebright R.H.;
RT "Transcription activation at class II CAP-dependent promoters: two
RT interactions between CAP and RNA polymerase.";
RL Cell 87:1123-1134(1996).
RN [15]
RP ADP-RIBOSYLATION AT ARG-265 (MICROBIAL INFECTION).
RX PubMed=4371081; DOI=10.1016/s0021-9258(19)42238-2;
RA Goff C.G.;
RT "Chemical structure of a modification of the Escherichia coli ribonucleic
RT acid polymerase alpha polypeptides induced by bacteriophage T4 infection.";
RL J. Biol. Chem. 249:6181-6190(1974).
RN [16]
RP ADP-RIBOSYLATION (MICROBIAL INFECTION).
RX PubMed=10634320;
RA Tiemann B., Depping R., Rueger W.;
RT "Overexpression, purification, and partial characterization of ADP-
RT ribosyltransferases modA and modB of bacteriophage T4.";
RL Gene Expr. 8:187-196(1999).
RN [17]
RP ADP-RIBOSYLATION (MICROBIAL INFECTION).
RX PubMed=15489438; DOI=10.1128/jb.186.21.7262-7272.2004;
RA Tiemann B., Depping R., Gineikiene E., Kaliniene L., Nivinskas R.,
RA Ruger W.;
RT "ModA and ModB, two ADP-ribosyltransferases encoded by bacteriophage T4:
RT catalytic properties and mutation analysis.";
RL J. Bacteriol. 186:7262-7272(2004).
RN [18]
RP ACETYLATION AT LYS-297 AND LYS-298.
RX PubMed=21696463; DOI=10.1111/j.1365-2958.2011.07742.x;
RA Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R.,
RA Wolfe A.J.;
RT "Involvement of protein acetylation in glucose-induced transcription of a
RT stress-responsive promoter.";
RL Mol. Microbiol. 81:1190-1204(2011).
RN [19]
RP STRUCTURE BY NMR OF 233-349.
RX PubMed=7491496; DOI=10.1126/science.270.5241.1495;
RA Jeon Y.H., Negishi T., Shirakawa M., Yamazaki T., Fujita N., Ishihama A.,
RA Kyogoku Y.;
RT "Solution structure of the activator contact domain of the RNA polymerase
RT alpha subunit.";
RL Science 270:1495-1497(1995).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-235.
RX PubMed=9657722; DOI=10.1126/science.281.5374.262;
RA Zhang G., Darst S.A.;
RT "Structure of the Escherichia coli RNA polymerase alpha subunit amino-
RT terminal domain.";
RL Science 281:262-266(1998).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 246-329 IN COMPLEX WITH DNA AND
RP CRP, INTERACTION WITH CRP, DNA-BINDING, AND SUBUNIT.
RX PubMed=12202833; DOI=10.1126/science.1076376;
RA Benoff B., Yang H., Lawson C.L., Parkinson G., Liu J., Blatter E.,
RA Ebright Y.W., Berman H.M., Ebright R.H.;
RT "Structural basis of transcription activation: the CAP-alpha CTD-DNA
RT complex.";
RL Science 297:1562-1566(2002).
RN [22] {ECO:0007744|PDB:3IYD}
RP STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) IN COMPLEX WITH RPOB;
RP RPOC; RPOD; RPOZ; CRP AND DNA, INTERACTION WITH CRP, DNA-BINDING, AND
RP SUBUNIT.
RX PubMed=19903881; DOI=10.1073/pnas.0908782106;
RA Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M., Arnold E.,
RA Ebright R.H., Lawson C.L.;
RT "Three-dimensional EM structure of an intact activator-dependent
RT transcription initiation complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009).
RN [23] {ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY}
RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) OF 2-329 IN COMPLEX WITH RPOB; RPOC;
RP RPOD; RPOZ AND SALINAMIDE A, FUNCTION, AND SUBUNIT.
RX PubMed=24843001; DOI=10.7554/elife.02451;
RA Degen D., Feng Y., Zhang Y., Ebright K.Y., Ebright Y.W., Gigliotti M.,
RA Vahedian-Movahed H., Mandal S., Talaue M., Connell N., Arnold E.,
RA Fenical W., Ebright R.H.;
RT "Transcription inhibition by the depsipeptide antibiotic salinamide A.";
RL Elife 3:e02451-e02451(2014).
RN [24] {ECO:0007744|PDB:6TQN, ECO:0007744|PDB:6TQO}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RRNA
RP TRANSCRIPTION-ELONGATION-ANTITERMINATION COMPLEXES WITH AND WITHOUT S4,
RP FUNCTION, AND SUBUNIT.
RX PubMed=32871103; DOI=10.1016/j.molcel.2020.08.010;
RA Huang Y.H., Hilal T., Loll B., Buerger J., Mielke T., Boettcher C.,
RA Said N., Wahl M.C.;
RT "Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone Machine
RT Required for Ribosome Biosynthesis.";
RL Mol. Cell 0:0-0(2020).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. This subunit plays an important role in
CC subunit assembly since its dimerization is the first step in the
CC sequential assembly of subunits to form the holoenzyme.
CC {ECO:0000269|PubMed:1646077, ECO:0000269|PubMed:24843001}.
CC -!- FUNCTION: Part of the processive rRNA transcription and antitermination
CC complex (rrnTAC). The complex forms an RNA-chaperone ring around the
CC RNA exit tunnel of RNAP. It supports rapid transcription and
CC antitermination of rRNA operons, cotranscriptional rRNA folding, and
CC annealing of distal rRNA regions to allow correct ribosome biogenesis.
CC {ECO:0000269|PubMed:32871103}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6;
CC -!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1
CC beta, 1 beta' and 1 omega subunit. When a sigma factor is associated
CC with the core the holoenzyme is formed, which can initiate
CC transcription. Both the N- and C-terminus interact with different
CC regions of transcriptional regulator CRP. The rRNA transcription and
CC antitermination complex (rrnTAC) consists of RNAP, NusA, NusB, NusE
CC (rpsJ), NusG, SubB, ribosomal protein S4, DNA and precursor rRNA; S4 is
CC more flexible than other subunits (PubMed:32871103).
CC {ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1646077,
CC ECO:0000269|PubMed:19903881, ECO:0000269|PubMed:2235479,
CC ECO:0000269|PubMed:24843001, ECO:0000269|PubMed:32871103}.
CC -!- INTERACTION:
CC P0A7Z4; P0ABQ0: coaBC; NbExp=2; IntAct=EBI-544985, EBI-548929;
CC P0A7Z4; P0AFF6: nusA; NbExp=7; IntAct=EBI-544985, EBI-551571;
CC P0A7Z4; P60422: rplB; NbExp=6; IntAct=EBI-544985, EBI-543515;
CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal
CC transcription, whereas the C-terminal domain is involved in interaction
CC with transcriptional regulators (such as CRP) and with upstream
CC promoter elements. {ECO:0000269|PubMed:1646077,
CC ECO:0000269|PubMed:2235479}.
CC -!- PTM: Acetylated on Lys-297 and Lys-298 in the presence of glucose. PatZ
CC controls acetylation of Lys-298 but not of Lys-297.
CC {ECO:0000269|PubMed:21696463}.
CC -!- PTM: (Microbial infection) ADP-ribosylated on both alpha subunits by
CC the phage T4 protein ModA (PubMed:10634320, PubMed:15489438). ADP-
CC ribosylated on only one of the alpha subunits by the phage T4 protein
CC Alt (PubMed:15489438). {ECO:0000269|PubMed:10634320,
CC ECO:0000269|PubMed:15489438}.
CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC {ECO:0000305}.
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DR EMBL; J01685; AAA24577.1; -; Genomic_DNA.
DR EMBL; X00766; CAA25337.1; -; Genomic_DNA.
DR EMBL; X02543; CAA26395.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58092.1; -; Genomic_DNA.
DR EMBL; X53843; CAA37838.1; -; Genomic_DNA.
DR EMBL; X53844; CAA37839.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76320.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77996.1; -; Genomic_DNA.
DR EMBL; V00353; CAA23646.1; -; Genomic_DNA.
DR EMBL; M29822; AAA24590.1; -; Genomic_DNA.
DR EMBL; M29823; AAA24592.1; -; Genomic_DNA.
DR EMBL; M29824; AAA24594.1; -; Genomic_DNA.
DR PIR; A22884; RNECA.
DR RefSeq; NP_417754.1; NC_000913.3.
DR RefSeq; WP_001162094.1; NZ_STEB01000038.1.
DR PDB; 1BDF; X-ray; 2.50 A; A/B/C/D=1-235.
DR PDB; 1COO; NMR; -; A=233-329.
DR PDB; 1LB2; X-ray; 3.10 A; B/E=246-329.
DR PDB; 1XS9; NMR; -; D=249-329.
DR PDB; 3IYD; EM; -; A/B=1-329.
DR PDB; 3K4G; X-ray; 2.05 A; A/B/C/D/E/F/G/H=245-329.
DR PDB; 3LU0; EM; -; A/B=1-329.
DR PDB; 3N4M; X-ray; 2.99 A; B/C=246-329.
DR PDB; 3N97; X-ray; 3.25 A; B/C=246-329.
DR PDB; 4JK1; X-ray; 3.90 A; A/B/F/G=1-329.
DR PDB; 4JK2; X-ray; 4.20 A; A/B/F/G=1-329.
DR PDB; 4KMU; X-ray; 3.85 A; A/B/F/G=1-329.
DR PDB; 4KN4; X-ray; 3.96 A; A/B/F/G=1-329.
DR PDB; 4KN7; X-ray; 3.69 A; A/B/F/G=1-329.
DR PDB; 4MEX; X-ray; 3.90 A; A/B/G/H=1-329.
DR PDB; 4MEY; X-ray; 3.95 A; A/B/G/H=1-329.
DR PDB; 4S20; X-ray; 4.70 A; A/B/F/G=1-329.
DR PDB; 4XSX; X-ray; 3.71 A; A/B/G/H=1-234.
DR PDB; 4XSY; X-ray; 4.01 A; A/B/G/H=1-234.
DR PDB; 4XSZ; X-ray; 3.68 A; A/B/G/H=1-234.
DR PDB; 4YG2; X-ray; 3.70 A; A/B/G/H=1-329.
DR PDB; 4YLN; X-ray; 5.50 A; A/B/G/H/M/N=1-235.
DR PDB; 4YLO; X-ray; 6.00 A; A/B/G/H/M/N=1-235.
DR PDB; 4YLP; X-ray; 5.50 A; A/B/G/H/M/N=1-235.
DR PDB; 4ZH2; X-ray; 4.20 A; A/B/G/H=2-329.
DR PDB; 4ZH3; X-ray; 4.08 A; A/B/G/H=2-329.
DR PDB; 4ZH4; X-ray; 3.99 A; A/B/G/H=2-329.
DR PDB; 5BYH; X-ray; 3.76 A; A/B=1-329.
DR PDB; 5CIZ; X-ray; 5.01 A; B=246-329.
DR PDB; 5EZK; X-ray; 8.50 A; A/B=1-329.
DR PDB; 5IPL; X-ray; 3.60 A; A/B=1-235.
DR PDB; 5IPM; X-ray; 4.20 A; A/B=1-235.
DR PDB; 5IPN; X-ray; 4.61 A; A/B=1-235.
DR PDB; 5MS0; EM; 9.80 A; A/B=1-329.
DR PDB; 5MY1; EM; 7.60 A; V/W=1-329.
DR PDB; 5NSR; EM; 3.80 A; A/B=1-329.
DR PDB; 5NSS; EM; 5.80 A; A/B=1-329.
DR PDB; 5NWT; X-ray; 3.76 A; A/B=1-329.
DR PDB; 5UAC; X-ray; 3.80 A; A/B/G/H=1-329.
DR PDB; 5UAG; X-ray; 3.40 A; A/B/G/H=1-320.
DR PDB; 5UAH; X-ray; 4.10 A; A/B/G/H=1-329.
DR PDB; 5UAJ; X-ray; 3.92 A; A/B/G/H=1-329.
DR PDB; 5UAL; X-ray; 3.89 A; A/B/G/H=1-329.
DR PDB; 5UAQ; X-ray; 3.60 A; A/B/G/H=1-329.
DR PDB; 5VSW; X-ray; 4.29 A; A/B/G/H=1-329.
DR PDB; 5VT0; EM; 3.78 A; G/H=1-234.
DR PDB; 5W1S; X-ray; 3.81 A; A/B/G/H=1-329.
DR PDB; 5W1T; X-ray; 4.50 A; A/B/G/H=1-329.
DR PDB; 6ALF; EM; 4.10 A; G/H=1-234.
DR PDB; 6ALG; EM; 3.70 A; G/H=1-234.
DR PDB; 6ALH; EM; 4.40 A; G/H=1-234.
DR PDB; 6ASX; EM; 3.80 A; G/H=1-234.
DR PDB; 6BJS; EM; 5.50 A; G/H=1-234.
DR PDB; 6BYU; X-ray; 3.60 A; A/B/G/H=1-329.
DR PDB; 6C6S; EM; 3.70 A; G/H=1-234.
DR PDB; 6C6T; EM; 3.50 A; G/H=1-234.
DR PDB; 6C6U; EM; 3.70 A; G/H=1-234.
DR PDB; 6C9Y; EM; 4.25 A; A/B=1-329.
DR PDB; 6CA0; EM; 5.75 A; A/B=1-329.
DR PDB; 6CUX; X-ray; 4.10 A; A/B/G/H=1-329.
DR PDB; 6FLP; EM; 4.10 A; A/B=1-329.
DR PDB; 6FLQ; EM; 4.10 A; A/B=1-329.
DR PDB; 6GFW; EM; 3.70 A; A/B=1-329.
DR PDB; 6GH5; EM; 3.40 A; A/B=1-329.
DR PDB; 6GH6; EM; 4.10 A; A/B=1-329.
DR PDB; 6JBQ; EM; 4.02 A; A/B=1-329.
DR PDB; 6JNX; EM; 4.08 A; A/B=1-329.
DR PDB; 6K4Y; EM; 3.79 A; A/B=1-329.
DR PDB; 6KJ6; EM; 3.80 A; A/B=1-329.
DR PDB; 6LDI; EM; 3.69 A; A/B=1-329.
DR PDB; 6N4C; EM; 17.00 A; A=6-321, B=6-315.
DR PDB; 6N57; EM; 3.70 A; G/H=1-329.
DR PDB; 6N58; EM; 3.78 A; G/H=1-329.
DR PDB; 6N60; X-ray; 3.68 A; A/B=1-234.
DR PDB; 6N61; X-ray; 3.25 A; A/B=1-234.
DR PDB; 6OMF; EM; 3.26 A; A/B=1-234.
DR PDB; 6OUL; EM; 3.40 A; G/H/R=1-329.
DR PDB; 6P18; EM; 3.50 A; A/B=1-329.
DR PDB; 6P19; EM; 3.80 A; A/B=1-329.
DR PDB; 6P1K; EM; 4.05 A; G/H=1-329.
DR PDB; 6PB4; EM; 4.35 A; A/B=1-329.
DR PDB; 6PB5; EM; 4.52 A; A/B=1-329.
DR PDB; 6PB6; EM; 4.29 A; A/B=1-329.
DR PDB; 6PMI; EM; 3.86 A; A/B=1-329.
DR PDB; 6PMJ; EM; 3.91 A; A/B=1-329.
DR PDB; 6PSQ; EM; 3.40 A; G/H/M=1-329.
DR PDB; 6PSR; EM; 3.40 A; G/H/M=1-329.
DR PDB; 6PSS; EM; 3.50 A; G/H/M=1-329.
DR PDB; 6PST; EM; 3.00 A; G/H/M=1-329.
DR PDB; 6PSU; EM; 3.90 A; G/H/M=1-329.
DR PDB; 6PSV; EM; 3.50 A; G/H/M=1-329.
DR PDB; 6PSW; EM; 3.70 A; G/H/M=1-329.
DR PDB; 6R9B; EM; 3.80 A; A/B=1-329.
DR PDB; 6R9G; EM; 3.70 A; A/B=1-329.
DR PDB; 6RH3; EM; 3.60 A; A/B=1-329.
DR PDB; 6RI7; EM; 3.90 A; A/B=1-329.
DR PDB; 6RI9; EM; 3.70 A; A/B=1-329.
DR PDB; 6RIN; EM; 3.70 A; A/B=1-329.
DR PDB; 6RIP; EM; 3.40 A; A/B=1-329.
DR PDB; 6TQN; EM; 3.80 A; U/V=1-329.
DR PDB; 6TQO; EM; 3.80 A; U/V=1-329.
DR PDB; 6UTW; X-ray; 3.85 A; AAA/BBB=1-235.
DR PDB; 6UTX; X-ray; 4.05 A; AAA/BBB=1-235.
DR PDB; 6UTY; X-ray; 4.15 A; AAA/BBB=1-235.
DR PDB; 6UU5; X-ray; 5.40 A; AAA/BBB=1-235.
DR PDB; 6UU6; X-ray; 4.20 A; AAA/BBB=1-235.
DR PDB; 6UU7; X-ray; 4.40 A; AAA/BBB=1-235.
DR PDB; 6UU8; X-ray; 4.40 A; AAA/BBB=1-235.
DR PDB; 6UUB; X-ray; 3.96 A; AAA/BBB=1-235.
DR PDB; 6VJS; X-ray; 4.02 A; A/B/F/G=1-329.
DR PDB; 6WMU; EM; 3.18 A; A/B=1-329.
DR PDB; 6X26; EM; 4.10 A; G/H=1-329.
DR PDB; 6X2F; EM; 4.00 A; G/H=1-329.
DR PDB; 6X2N; EM; 3.90 A; G/H=1-329.
DR PDB; 6X43; EM; 3.60 A; G/H=1-329.
DR PDB; 6X4W; EM; 3.80 A; G/H=1-329.
DR PDB; 6X4Y; EM; 3.60 A; G/H=1-329.
DR PDB; 6X50; EM; 3.30 A; G/H=1-329.
DR PDB; 6XAS; EM; 3.80 A; H/K=1-329.
DR PDB; 6XAV; EM; 7.70 A; H/K=1-329.
DR PDB; 6XH7; EM; 3.90 A; A/B=1-329.
DR PDB; 6XH8; EM; 4.10 A; A/B=1-329.
DR PDB; 6XL5; EM; 2.50 A; A/B=1-329.
DR PDB; 6XL9; EM; 2.50 A; A/B=1-329.
DR PDB; 6XLJ; EM; 2.70 A; A/B=1-329.
DR PDB; 6XLL; EM; 2.70 A; A/B=1-329.
DR PDB; 6XLM; EM; 3.20 A; A/B=1-329.
DR PDB; 6XLN; EM; 2.80 A; A/B=1-329.
DR PDB; 6Z9P; EM; 3.90 A; U/V=1-329.
DR PDB; 6Z9Q; EM; 5.70 A; U/V=1-329.
DR PDB; 6Z9R; EM; 4.10 A; U/V=1-329.
DR PDB; 6Z9S; EM; 4.40 A; U/V=1-329.
DR PDB; 6Z9T; EM; 4.10 A; U/V=1-329.
DR PDB; 6ZTJ; EM; 3.40 A; CA/CB=1-329.
DR PDB; 6ZTL; EM; 3.50 A; CA/CB=1-329.
DR PDB; 6ZTM; EM; 3.30 A; CA/CB=1-329.
DR PDB; 6ZTN; EM; 3.90 A; CA/CB=1-329.
DR PDB; 6ZTO; EM; 3.00 A; CA/CB=1-329.
DR PDB; 6ZTP; EM; 3.00 A; CA/CB=1-329.
DR PDB; 6ZU1; EM; 3.00 A; CA/CB=1-329.
DR PDB; 7ADB; EM; 4.40 A; U/V=1-329.
DR PDB; 7ADC; EM; 4.00 A; U/V=1-329.
DR PDB; 7ADD; EM; 4.30 A; U/V=1-329.
DR PDB; 7ADE; EM; 4.20 A; U/V=1-329.
DR PDB; 7BEF; EM; 4.50 A; A/B=1-329.
DR PDB; 7BEG; EM; 4.20 A; A/B=1-329.
DR PDB; 7C17; EM; 4.22 A; A/B=1-329.
DR PDB; 7C97; EM; 3.68 A; A/B/K=1-329.
DR PDB; 7CHW; EM; 3.58 A; A/B/K=1-329.
DR PDB; 7KHB; EM; 3.53 A; A/B=1-329.
DR PDB; 7KHC; EM; 4.14 A; A/B=1-329.
DR PDB; 7KHE; EM; 3.58 A; A/B=1-236.
DR PDB; 7KHI; EM; 3.62 A; A/B=1-236.
DR PDB; 7M8E; EM; 3.40 A; A/B=1-329.
DR PDB; 7MKD; EM; 3.20 A; G/H/R=1-329.
DR PDB; 7MKE; EM; 3.70 A; G/H=1-329.
DR PDB; 7MKI; EM; 3.50 A; G/H=1-329.
DR PDB; 7MKJ; EM; 2.90 A; G/H/R=1-329.
DR PDB; 7MKN; EM; 3.30 A; A/B=1-237.
DR PDB; 7MKO; EM; 3.15 A; A/B=1-237.
DR PDB; 7MKP; EM; 3.41 A; A/B=1-237.
DR PDB; 7MKQ; EM; 4.80 A; A/B=1-237.
DR PDB; 7PY0; EM; 4.50 A; A/B=1-329.
DR PDB; 7PY1; EM; 3.80 A; A/B=1-329.
DR PDB; 7PY3; EM; 3.80 A; A/B=1-329.
DR PDB; 7PY5; EM; 3.90 A; A/B=1-329.
DR PDB; 7PY6; EM; 4.10 A; A/B=1-329.
DR PDB; 7PY7; EM; 4.10 A; A/B=1-329.
DR PDB; 7PY8; EM; 3.80 A; A/B=1-329.
DR PDB; 7PYJ; EM; 4.20 A; A/B=1-329.
DR PDB; 7PYK; EM; 4.10 A; A/B=1-329.
DR PDB; 7Q0J; EM; 4.30 A; A/B=1-329.
DR PDB; 7Q0K; EM; 4.00 A; A/B=1-329.
DR PDBsum; 1BDF; -.
DR PDBsum; 1COO; -.
DR PDBsum; 1LB2; -.
DR PDBsum; 1XS9; -.
DR PDBsum; 3IYD; -.
DR PDBsum; 3K4G; -.
DR PDBsum; 3LU0; -.
DR PDBsum; 3N4M; -.
DR PDBsum; 3N97; -.
DR PDBsum; 4JK1; -.
DR PDBsum; 4JK2; -.
DR PDBsum; 4KMU; -.
DR PDBsum; 4KN4; -.
DR PDBsum; 4KN7; -.
DR PDBsum; 4MEX; -.
DR PDBsum; 4MEY; -.
DR PDBsum; 4S20; -.
DR PDBsum; 4XSX; -.
DR PDBsum; 4XSY; -.
DR PDBsum; 4XSZ; -.
DR PDBsum; 4YG2; -.
DR PDBsum; 4YLN; -.
DR PDBsum; 4YLO; -.
DR PDBsum; 4YLP; -.
DR PDBsum; 4ZH2; -.
DR PDBsum; 4ZH3; -.
DR PDBsum; 4ZH4; -.
DR PDBsum; 5BYH; -.
DR PDBsum; 5CIZ; -.
DR PDBsum; 5EZK; -.
DR PDBsum; 5IPL; -.
DR PDBsum; 5IPM; -.
DR PDBsum; 5IPN; -.
DR PDBsum; 5MS0; -.
DR PDBsum; 5MY1; -.
DR PDBsum; 5NSR; -.
DR PDBsum; 5NSS; -.
DR PDBsum; 5NWT; -.
DR PDBsum; 5UAC; -.
DR PDBsum; 5UAG; -.
DR PDBsum; 5UAH; -.
DR PDBsum; 5UAJ; -.
DR PDBsum; 5UAL; -.
DR PDBsum; 5UAQ; -.
DR PDBsum; 5VSW; -.
DR PDBsum; 5VT0; -.
DR PDBsum; 5W1S; -.
DR PDBsum; 5W1T; -.
DR PDBsum; 6ALF; -.
DR PDBsum; 6ALG; -.
DR PDBsum; 6ALH; -.
DR PDBsum; 6ASX; -.
DR PDBsum; 6BJS; -.
DR PDBsum; 6BYU; -.
DR PDBsum; 6C6S; -.
DR PDBsum; 6C6T; -.
DR PDBsum; 6C6U; -.
DR PDBsum; 6C9Y; -.
DR PDBsum; 6CA0; -.
DR PDBsum; 6CUX; -.
DR PDBsum; 6FLP; -.
DR PDBsum; 6FLQ; -.
DR PDBsum; 6GFW; -.
DR PDBsum; 6GH5; -.
DR PDBsum; 6GH6; -.
DR PDBsum; 6JBQ; -.
DR PDBsum; 6JNX; -.
DR PDBsum; 6K4Y; -.
DR PDBsum; 6KJ6; -.
DR PDBsum; 6LDI; -.
DR PDBsum; 6N4C; -.
DR PDBsum; 6N57; -.
DR PDBsum; 6N58; -.
DR PDBsum; 6N60; -.
DR PDBsum; 6N61; -.
DR PDBsum; 6OMF; -.
DR PDBsum; 6OUL; -.
DR PDBsum; 6P18; -.
DR PDBsum; 6P19; -.
DR PDBsum; 6P1K; -.
DR PDBsum; 6PB4; -.
DR PDBsum; 6PB5; -.
DR PDBsum; 6PB6; -.
DR PDBsum; 6PMI; -.
DR PDBsum; 6PMJ; -.
DR PDBsum; 6PSQ; -.
DR PDBsum; 6PSR; -.
DR PDBsum; 6PSS; -.
DR PDBsum; 6PST; -.
DR PDBsum; 6PSU; -.
DR PDBsum; 6PSV; -.
DR PDBsum; 6PSW; -.
DR PDBsum; 6R9B; -.
DR PDBsum; 6R9G; -.
DR PDBsum; 6RH3; -.
DR PDBsum; 6RI7; -.
DR PDBsum; 6RI9; -.
DR PDBsum; 6RIN; -.
DR PDBsum; 6RIP; -.
DR PDBsum; 6TQN; -.
DR PDBsum; 6TQO; -.
DR PDBsum; 6UTW; -.
DR PDBsum; 6UTX; -.
DR PDBsum; 6UTY; -.
DR PDBsum; 6UU5; -.
DR PDBsum; 6UU6; -.
DR PDBsum; 6UU7; -.
DR PDBsum; 6UU8; -.
DR PDBsum; 6UUB; -.
DR PDBsum; 6VJS; -.
DR PDBsum; 6WMU; -.
DR PDBsum; 6X26; -.
DR PDBsum; 6X2F; -.
DR PDBsum; 6X2N; -.
DR PDBsum; 6X43; -.
DR PDBsum; 6X4W; -.
DR PDBsum; 6X4Y; -.
DR PDBsum; 6X50; -.
DR PDBsum; 6XAS; -.
DR PDBsum; 6XAV; -.
DR PDBsum; 6XH7; -.
DR PDBsum; 6XH8; -.
DR PDBsum; 6XL5; -.
DR PDBsum; 6XL9; -.
DR PDBsum; 6XLJ; -.
DR PDBsum; 6XLL; -.
DR PDBsum; 6XLM; -.
DR PDBsum; 6XLN; -.
DR PDBsum; 6Z9P; -.
DR PDBsum; 6Z9Q; -.
DR PDBsum; 6Z9R; -.
DR PDBsum; 6Z9S; -.
DR PDBsum; 6Z9T; -.
DR PDBsum; 6ZTJ; -.
DR PDBsum; 6ZTL; -.
DR PDBsum; 6ZTM; -.
DR PDBsum; 6ZTN; -.
DR PDBsum; 6ZTO; -.
DR PDBsum; 6ZTP; -.
DR PDBsum; 6ZU1; -.
DR PDBsum; 7ADB; -.
DR PDBsum; 7ADC; -.
DR PDBsum; 7ADD; -.
DR PDBsum; 7ADE; -.
DR PDBsum; 7BEF; -.
DR PDBsum; 7BEG; -.
DR PDBsum; 7C17; -.
DR PDBsum; 7C97; -.
DR PDBsum; 7CHW; -.
DR PDBsum; 7KHB; -.
DR PDBsum; 7KHC; -.
DR PDBsum; 7KHE; -.
DR PDBsum; 7KHI; -.
DR PDBsum; 7M8E; -.
DR PDBsum; 7MKD; -.
DR PDBsum; 7MKE; -.
DR PDBsum; 7MKI; -.
DR PDBsum; 7MKJ; -.
DR PDBsum; 7MKN; -.
DR PDBsum; 7MKO; -.
DR PDBsum; 7MKP; -.
DR PDBsum; 7MKQ; -.
DR PDBsum; 7PY0; -.
DR PDBsum; 7PY1; -.
DR PDBsum; 7PY3; -.
DR PDBsum; 7PY5; -.
DR PDBsum; 7PY6; -.
DR PDBsum; 7PY7; -.
DR PDBsum; 7PY8; -.
DR PDBsum; 7PYJ; -.
DR PDBsum; 7PYK; -.
DR PDBsum; 7Q0J; -.
DR PDBsum; 7Q0K; -.
DR AlphaFoldDB; P0A7Z4; -.
DR SMR; P0A7Z4; -.
DR BioGRID; 4263398; 114.
DR BioGRID; 852106; 1.
DR ComplexPortal; CPX-4881; DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant.
DR ComplexPortal; CPX-4883; DNA-directed RNA polymerase holoenzyme complex, SigmaS variant.
DR ComplexPortal; CPX-4884; DNA-directed RNA polymerase holoenzyme complex, Sigma54 variant.
DR ComplexPortal; CPX-4885; DNA-directed RNA polymerase holoenzyme complex, SigmaE variant.
DR ComplexPortal; CPX-4886; DNA-directed RNA polymerase holoenzyme complex, SigmaF variant.
DR ComplexPortal; CPX-4887; DNA-directed RNA polymerase holoenzyme complex, SigmaH variant.
DR ComplexPortal; CPX-4888; DNA-directed RNA polymerase holoenzyme complex, Sigma fecI variant.
DR ComplexPortal; CPX-5674; Transcription elongation complex.
DR ComplexPortal; CPX-5780; lambdaN-dependent processive transcription antitermination complex.
DR DIP; DIP-35879N; -.
DR IntAct; P0A7Z4; 91.
DR MINT; P0A7Z4; -.
DR STRING; 511145.b3295; -.
DR BindingDB; P0A7Z4; -.
DR ChEMBL; CHEMBL2364672; -.
DR ChEMBL; CHEMBL4296169; -.
DR DrugBank; DB00615; Rifabutin.
DR DrugBank; DB11753; Rifamycin.
DR DrugCentral; P0A7Z4; -.
DR iPTMnet; P0A7Z4; -.
DR SWISS-2DPAGE; P0A7Z4; -.
DR jPOST; P0A7Z4; -.
DR PaxDb; P0A7Z4; -.
DR PRIDE; P0A7Z4; -.
DR EnsemblBacteria; AAC76320; AAC76320; b3295.
DR EnsemblBacteria; BAE77996; BAE77996; BAE77996.
DR GeneID; 67415336; -.
DR GeneID; 947794; -.
DR KEGG; ecj:JW3257; -.
DR KEGG; eco:b3295; -.
DR PATRIC; fig|1411691.4.peg.3436; -.
DR EchoBASE; EB0886; -.
DR eggNOG; COG0202; Bacteria.
DR HOGENOM; CLU_053084_0_0_6; -.
DR InParanoid; P0A7Z4; -.
DR OMA; LMKFRNF; -.
DR PhylomeDB; P0A7Z4; -.
DR BioCyc; EcoCyc:EG10893-MON; -.
DR BioCyc; MetaCyc:EG10893-MON; -.
DR BRENDA; 2.7.7.6; 2026.
DR EvolutionaryTrace; P0A7Z4; -.
DR PRO; PR:P0A7Z4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0000345; C:cytosolic DNA-directed RNA polymerase complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IC:ComplexPortal.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IC:ComplexPortal.
DR GO; GO:0048870; P:cell motility; IC:ComplexPortal.
DR GO; GO:0036460; P:cellular response to cell envelope stress; IC:ComplexPortal.
DR GO; GO:0055072; P:iron ion homeostasis; IC:ComplexPortal.
DR GO; GO:0042128; P:nitrate assimilation; IC:ComplexPortal.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IC:ComplexPortal.
DR GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; IDA:ComplexPortal.
DR GO; GO:0009408; P:response to heat; IC:ComplexPortal.
DR GO; GO:0090605; P:submerged biofilm formation; IC:ComplexPortal.
DR GO; GO:0031564; P:transcription antitermination; IDA:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00059; RNApol_bact_RpoA; 1.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR011773; DNA-dir_RpoA.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR011260; RNAP_asu_C.
DR InterPro; IPR036643; RNApol_insert_sf.
DR PANTHER; PTHR32108; PTHR32108; 1.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF03118; RNA_pol_A_CTD; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR TIGRFAMs; TIGR02027; rpoA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Direct protein sequencing;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..329
FT /note="DNA-directed RNA polymerase subunit alpha"
FT /id="PRO_0000175304"
FT REGION 1..235
FT /note="Alpha N-terminal domain (alpha-NTD)"
FT REGION 162..165
FT /note="Required for interaction with Crp at class II
FT promoters"
FT REGION 249..329
FT /note="Alpha C-terminal domain (alpha-CTD); not required
FT for RNAP assembly or function"
FT MOD_RES 265
FT /note="ADP-ribosylarginine"
FT /evidence="ECO:0000269|PubMed:4371081"
FT MOD_RES 297
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:21696463"
FT MOD_RES 298
FT /note="N6-acetyllysine; by PatZ"
FT /evidence="ECO:0000269|PubMed:21696463"
FT MUTAGEN 45
FT /note="R->C: In rpoA112; temperature-sensitive, blocks RNA
FT polymerase assembly."
FT /evidence="ECO:0000269|PubMed:2235479"
FT MUTAGEN 162..165
FT /note="EEDE->AAAA: 5-fold decrease in CRP-class II
FT promoter-dependent transcription."
FT /evidence="ECO:0000269|PubMed:8978616"
FT MUTAGEN 165
FT /note="E->K: 5-fold decrease in CRP-class II promoter-
FT dependent transcription."
FT /evidence="ECO:0000269|PubMed:8978616"
FT MUTAGEN 191
FT /note="R->C: In rpoA101; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:2235479"
FT CONFLICT 4
FT /note="S -> N (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="N -> T (in Ref. 4; CAA26395)"
FT /evidence="ECO:0000305"
FT STRAND 13..32
FT /evidence="ECO:0007829|PDB:1BDF"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:1BDF"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:1BDF"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1BDF"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:1BDF"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 96..111
FT /evidence="ECO:0007829|PDB:1BDF"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1BDF"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1BDF"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1BDF"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6XLL"
FT STRAND 139..148
FT /evidence="ECO:0007829|PDB:1BDF"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1BDF"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1BDF"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6OUL"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6XL5"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6PST"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:1BDF"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:6OUL"
FT STRAND 196..207
FT /evidence="ECO:0007829|PDB:1BDF"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1BDF"
FT HELIX 213..227
FT /evidence="ECO:0007829|PDB:1BDF"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:1BDF"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:3K4G"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:3K4G"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:3K4G"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:3N4M"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:3K4G"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:3K4G"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1XS9"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1XS9"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:3K4G"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:3K4G"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:3K4G"
SQ SEQUENCE 329 AA; 36512 MW; 12A14B75A3CAEA19 CRC64;
MQGSVTEFLK PRLVDIEQVS STHAKVTLEP LERGFGHTLG NALRRILLSS MPGCAVTEVE
IDGVLHEYST KEGVQEDILE ILLNLKGLAV RVQGKDEVIL TLNKSGIGPV TAADITHDGD
VEIVKPQHVI CHLTDENASI SMRIKVQRGR GYVPASTRIH SEEDERPIGR LLVDACYSPV
ERIAYNVEAA RVEQRTDLDK LVIEMETNGT IDPEEAIRRA ATILAEQLEA FVDLRDVRQP
EVKEEKPEFD PILLRPVDDL ELTVRSANCL KAEAIHYIGD LVQRTEVELL KTPNLGKKSL
TEIKDVLASR GLSLGMRLEN WPPASIADE
